Improved energy bound accuracy enhances the efficiency of continuous protein design.

ABSTRACT: Flexibility and dynamics are important for protein function and a protein's ability to accommodate amino acid substitutions. However, when computational protein design algorithms search over protein structures, the allowed flexibility is often reduced to a relatively small set of discrete side-chain and backbone conformations. While simplifications in scoring functions and protein flexibility are currently necessary to computationally search the vast protein sequence and conformational space, a rigid representation of a protein causes the search to become brittle and miss low-energy structures. Continuous rotamers more closely represent the allowed movement of a side chain within its torsional well and have been successfully incorporated into the protein design framework to design biomedic

SUBMITTER: Roberts KE 

PROVIDER: S-EPMC4526210 | biostudies-literature | 2015 Jun

REPOSITORIES: biostudies-literature